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Yorodumi- PDB-6vhq: Crystal structure of Bacillus subtilis levansucrase (D86A/E342A) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6vhq | ||||||||||||
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Title | Crystal structure of Bacillus subtilis levansucrase (D86A/E342A) in complex with oligosaccharides | ||||||||||||
Components | Glycoside hydrolase family 68 protein | ||||||||||||
Keywords | TRANSFERASE / Levansucrase / Glycoside hydrolase / Levan / Fructose polymers | ||||||||||||
Function / homology | Function and homology information levansucrase / levansucrase activity / carbohydrate utilization / extracellular region Similarity search - Function | ||||||||||||
Biological species | Bacillus subtilis (bacteria) | ||||||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.047 Å | ||||||||||||
Authors | Diaz-Vilchis, A. / Raga-Carbajal, E. / Rojas-Trejo, S. / Olvera, C. / Rudino-Pinera, E. | ||||||||||||
Funding support | Mexico, 3items
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Citation | Journal: J.Biol.Chem. / Year: 2020 Title: The molecular basis of the nonprocessive elongation mechanism in levansucrases. Authors: Raga-Carbajal, E. / Diaz-Vilchis, A. / Rojas-Trejo, S.P. / Rudino-Pinera, E. / Olvera, C. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6vhq.cif.gz | 209.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6vhq.ent.gz | 165.4 KB | Display | PDB format |
PDBx/mmJSON format | 6vhq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vh/6vhq ftp://data.pdbj.org/pub/pdb/validation_reports/vh/6vhq | HTTPS FTP |
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-Related structure data
Related structure data | 1oygS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 52360.797 Da / Num. of mol.: 2 / Mutation: D86A, E342A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) Gene: sacB, B4417_3269, ETA10_18085, ETL41_09350, FVD40_16900 Production host: Escherichia coli BL21 (bacteria) / References: UniProt: A0PFL2, UniProt: P05655*PLUS |
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-Sugars , 2 types, 4 molecules
#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | beta-D-fructofuranose-(2-6)-beta-D-fructofuranose / levanbiose | |
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-Non-polymers , 3 types, 551 molecules
#4: Chemical | #5: Chemical | ChemComp-BR / #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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Nonpolymer details | The entry contains the oligosaccharide levanhexaose, a 6 fructose units bound by beta2-6 glycosidic bonds |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.22 % |
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Crystal grow | Temperature: 291 K / Method: microbatch / pH: 6 / Details: 30 % w/v PEG 2000 MME and 150 mM Potassium Bromide |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å |
Detector | Type: DECTRIS PILATUS 200K / Detector: PIXEL / Date: Aug 10, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.047→35.205 Å / Num. obs: 53175 / % possible obs: 99.99 % / Observed criterion σ(I): 3.5 / Redundancy: 2.7 % / Biso Wilson estimate: 25.1 Å2 / Rmerge(I) obs: 0.048 / Net I/σ(I): 23.9 |
Reflection shell | Resolution: 2.047→2.09 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.526 / Mean I/σ(I) obs: 3.5 / Num. unique obs: 5145 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1OYG Resolution: 2.047→35.205 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 94.72 Å2 / Biso mean: 28.2683 Å2 / Biso min: 7.12 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.047→35.205 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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